Classification of the insulin-like growth factor binding proteins into three distinct categories according to their binding specificities

Forbes, Briony E.; Szabó, László; Baxter, Robert C.; Ballard, F. J.; Jc, Wallace

doi:10.1016/s0006-291x(88)80032-9

Cited by 76 publications

(41 citation statements)

References 17 publications

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“…Furthermore, the IC50 value of IGFBP-1 in the binding experiment (0.32 nM) is similar to that obtained in the inhibition of estradiol release by IGFBP-1 (0.27 nM). The capacity of IGFBPs to inhibit IGF action has been corre lated with the affinity for the ligand, and the reported IC50 value of IGF-I for IGFBP-1 was 0.3 nM [37], similar to the values obtained in this study. These results strongly suggest that IGFBP-1 inhibits IGF-I-mediated estradiol release by preventing access of IGF-I to receptors in luteinizing granulosa cells.…”

Section: Igf-i (Log M)supporting

confidence: 88%

Regulation and Physiological Role of Insulin-Like-Growth-Factor-Binding Protein-1 in Human Granulosa Cells

et al. 1994

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The present study was undertaken to elucidate the physiological role and the regulation of insulin-like growth factor (IGF)-binding protein-1 (IGFBP-1) in human luteinizing granulosa cells. IGFBP-1 abolished IGF-I-stimulated estradiol production by luteinizing granulosa cells in a dose-dependent manner with a 50% inhibitory concentration (IC₅₀) of 0.27 nM. Similarly, IGFBP-1 inhibited ¹²⁵I-IGF-I binding to granulosa cells. IGFBP-1 was identified by Western immunoblot and specific enzyme immunoassay in the granulosa-cell-conditioned medium after 24 h culture. Immunoreactive IGFBP-1 released into the medium was inhibited by both IGF-I and follicle-stimulating hormone dose-dependently with an IC_5o of 0.14 and 0.13 nM, respectively, while human chorionic gonadotropin-stimulated IGFBP-1 release with a 50% effective dose (ED₅₀) of 0.6 nM. These results suggest that IGFBP-1 is involved in follicular development and granulosa cell differentiation in the human ovary and that gonadotropins may influence IGF-I action by modifying IGFBP-1 levels within the ovary.

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Section: Igf-i (Log M)supporting

confidence: 88%

Regulation and Physiological Role of Insulin-Like-Growth-Factor-Binding Protein-1 in Human Granulosa Cells

et al. 1994

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“…Yet when bIGFBP-2 was iodinated alone, the loss in binding affinity for IGF-I was 2-fold more severe than that observed for IGF-II. This result was of interest considering the difference in relative affinity of bIGFBP-2 for IGF-II over IGF-I, which has been reported to be 4-fold (11) and as high as 20-fold (24,34). Therefore, Tyr 60 may influence the binding of IGF-I more strongly than IGF-II.…”

Section: Discussionmentioning

confidence: 93%

The Insulin-like Growth Factor (IGF) Binding Site of Bovine Insulin-like Growth Factor Binding Protein-2 (bIGFBP-2) Probed by Iodination

Hobba

Forbes

Parkinson

et al. 1996

Journal of Biological Chemistry

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“…The function of KAZALD1 in dental development and bone regeneration was investigated only recently and, thus far, its biological function is unknown (17). The KAZALD1 insulin-like factor binding domain has high affinity for insulin-like growth factors, while the Kazal domain contains sequence and structural homology to serine proteases and follistatins (15). The immunoglobulin-like domain appears to have a molecular binding function perhaps regulating cell adhesion and extracellular ligand binding (16), and is associated with regions of matrix mineralization (17).…”

Section: Discussionmentioning

confidence: 99%

Epigenetic silencing of KAZALD1 confers a better prognosis and is associated with malignant transformation/progression in glioma

WANG¹,

Feng²,

Bao³

et al. 2013

Oncology Reports

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Abstract.In order to more thoroughly analyze aberrant DNA methylation in glioma, we applied a large cohort methylation microarray including 119 glioma samples. Six genes, ADCY1, KAZALD1, KLF4, SLMAP, TETRAN and TP53INP1, were screened out through significance analysis of microarray (SAM), survival Cox-regression and certain other pre-set conditions. We focused on the KAZALD1 oncogene. KAZALD1, also known as IGFBP-rP10, belongs to the IGFBP family. We found that KAZALD1 was hypomethylated in highgrade glioma (anaplastic gliomas and glioblastomas) compared to low-grade glioma (astrocytoma, oligodendrocytoma and oligoastrocytoma) using methylation microarrays (P<0.001). Immunohistochemistry (IHC) of 91 glioma samples showed that the KAZALD1 expression scores of high-grade glioma samples were higher compared to the scores of low-grade gliomas (P<0.001). In high-grade gliomas, overall survival (OS) was shorter for patients with KAZALD1 hypomethylation or overexpression compared to those without. Decreased KAZALD1 expression in glioma inhibited cell proliferation and invasion both in vitro and in vivo. On the basis of these observations and the results from subset analysis, it is reasonable to conclude that KAZALD1 promoter hypomethylation is an important prognostic biomarker in glioma. KAZALD1 promotes glioma malignant progression through invasion and proliferation.

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Classification of the insulin-like growth factor binding proteins into three distinct categories according to their binding specificities

Cited by 76 publications

References 17 publications

Regulation and Physiological Role of Insulin-Like-Growth-Factor-Binding Protein-1 in Human Granulosa Cells

Regulation and Physiological Role of Insulin-Like-Growth-Factor-Binding Protein-1 in Human Granulosa Cells

The Insulin-like Growth Factor (IGF) Binding Site of Bovine Insulin-like Growth Factor Binding Protein-2 (bIGFBP-2) Probed by Iodination

Epigenetic silencing of KAZALD1 confers a better prognosis and is associated with malignant transformation/progression in glioma

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